Recombinant Mouse F-Spondin/SPON1 Protein, CF

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse F-Spondin/SPON1 Protein, CF Summary

• Details of Functionality: Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons. Able to significantly enhance neurite outgrowth when immobilized at 1.25‑5.0 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse F-Spondin/SPON1 protein
  Leu27-Cys807
• Accession #: Q8VCC9
• N-terminal Sequence: Leu27
• Protein/Peptide Type: Recombinant Proteins
• Gene: Spon1
• Purity: >90%, by SDS-PAGE with silver staining
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 88.2 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 105-115 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >90%, by SDS-PAGE with silver staining
• Reconstitution Instructions: Reconstitute at 300 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse F-Spondin/SPON1 Protein, CF

• FSpondin
• F-Spondin
• KIAA0762VSGP/F-spondin
• MGC10724
• SPON1
• spondin 1, (f-spondin) extracellular matrix protein
• spondin 1, extracellular matrix protein
• spondin-1
• Vascular smooth muscle cell growth-promoting factor
• VSGP

Background

F‑Spondin (floor plate and thrombospondin homology), also called Spondin‑1, SPON1 or VSGP (vascular smooth muscle growth‑promoting factor), is an approximately 110 kDa secreted glycoprotein that is a member of a subgroup of TSR (thrombospondin) molecules that are either membrane‑bound or associated with the extracellular matrix (ECM) (1‑3). Mouse F‑Spondin is synthesized as an 807 amino acid (aa) precursor with a 779 aa mature region that includes an N‑terminal reelin‑like domain, an F‑spondin (FS) domain, and six C‑terminal thrombospondin (TSP) type I repeats (1‑3). Mature mouse F‑Spondin shares 99% aa sequence identity with rat and 97% with human, bovine and canine F‑Spondin. TSP 5 and 6 bind ECM, while TSP 1‑4 plus the FS domain may mediate repulsive activity on motor neurons and outgrowth promoting activity on sensory neurons during development or after injury (2‑5). Crystal structure indicates that the reelin‑like domain binds heparin and may mediate weak dimerization (6). Plasmin cleavage generates a diffusible 95 kDa, 656 aa F‑spondin that lacks TSP 5 and 6, while non‑plasmin cleavage between the FS segment and the first TSP repeat generates 60 kDa and 50 kDa fragments (3, 4, 7). F‑Spondin shows unusual C‑mannosylation and O‑fucosylation within the TSP repeats (3). Mammalian cells expressing F‑spondin include floor plate epithelium, ventral motor neurons, Schwann cells, fibroblasts, hippocampal pyramidal cells, endothelial cells, vascular smooth muscle cells and some tumor cells (2‑5, 8). F‑Spondin can either tether cells to the ECM or interfere with integrin adhesion, thus either blocking or allowing nerve or vascular endothelial cell migration (3, 9). It binds beta ‑amyloid fibrils and inhibits beta ‑secretase cleavage, thus reducing A beta  plaque deposition associated with Alzheimer’s disease (10, 11). F‑Spondin is also reported to inhibit differentiation or migration during angiogenesis (affecting endothelial cells) and bone development (affecting osteoclast and chondrocyte precursors) (3, 9, 12, 13).

1. Miyamoto, K. et al. (2001) Arch. Biochem. Biophys. 390:93.
2. Klar, A. et al. (1992) Cell 69:95.
3. Feinstein, Y. and A. Klar (2004) Int. J. Biochem. Cell Biol. 36:975.
4. Burstyn-Cohen, T. et al. (1998) J. Neurosci. 18:8875.
5. Feinstein, Y. et al. (1999) Development 126:3637.
6. Tan, K. et al. (2008) J. Mol. Biol. 381:1213.
7. Tzarfaty-Majar, V. et al. (2001) J. Biol. Chem. 276:28233.
8. Pyle-Chenault, R.A. et al. (2005) Tumor Biol. 26:245.
9. Terai, Y. et al. (2001) J. Cell Physiol. 188:394.
10. Ho, A. and T.C. Sudhof (2004) Proc. Natl. Acad. Sci. USA 101:2548.
11. Hafez, D.M. et al. (2012) Neuroscience 223:465.
12. Palmer, G.D. et al. (2010) J. Orthop. Res. 28:1323.
13. Oka, H. et al. (2011) J. Periodontol. 82:1776.

Publications for F-Spondin/SPON1 (7950-SP)(1)

Publication using 7950-SP

• Whately, KM;Sengottuvel, N;Edatt, L;Srivastava, S;Woods, AT;Tsai, YS;Porrello, A;Zimmerman, MP;Chack, AC;Jefferys, SR;Yacovone, G;Kim, DJ;Dudley, AC;Amelio, AL;Pecot, CV; Spon1+ inflammatory monocytes promote collagen remodeling and lung cancer metastasis through lipoprotein receptor 8 signaling JCI insight 2024-05-08 [PMID: 38716730] (Bioassay, Mouse)

Bioinformatics

• Gene Symbol: Spon1
• Uniprot:
  • Q8VCC9()